Controlling catalytic activity through the non-covalent organization and assembly of molecules in a precise arrangement is at the heart of many biological processes and remains a challenge in supra-molecular nano-architectures. Proteins, simply stated, achieve this through a chain of amino acids that fold into a three-dimensional structure that in turn governs the molecules activity. Achieving complex biologically inspired reactivity in synthetic materials remains a challenge because of the need to simultaneously balance properties that lead to supramolecular assembly while maintaining precise molecular control near the catalytic active site. Peptide-amphiphiles, a class of supramolecular bio-based materials typically employed in regenerative medicine, provide an impressively simple solution to this problem. (1-3) The peptide serves as a scaffold with recognition, structural, and functional sites. The structural region guides assembly while the functional site, typically a modified or unnatural amino acid or sequence of amino acids, is used in mineralization or catalysis. (4-9) The peptide component, however, is highly underutilized and can be further programmed to incorporate function, ultimately generating a protein-like catalytic material. (10,11) However, peptide-amphiphile like many implanted biomaterials run into the problem of producing an inflammatory response due to damaged tissue produced from material implementation and often hinder the efficacy of the material.